| Literature DB >> 15502327 |
Nana Yokochi1, Yu Yoshikane, Toshiharu Yagi, Masayuki Yamasaki, Bunzo Mikami.
Abstract
Pyridoxal 4-dehydrogenase (PLDH; EC 1.1.107) is the second enzyme in the bacterial degradation pathway I of vitamin B(6), which catalyzes the oxidation of pyridoxal to 4-pyridoxolactone using NAD(+). PLDH from Microbacterium luteolum, a dimeric protein with a subunit molecular weight of 38 kDa, was crystallized at 277 K in a drop solution comprising 15%(w/v) polyethylene glycol 4000, 0.15 M sodium acetate, 7.5 mM n-octyl-beta-D-glucoside and 0.075 M Tris-HCl pH 7.5 by the sitting-drop vapour-diffusion method. The crystals were monoclinic and belonged to space group C2, with unit-cell parameters a = 107.0, b = 56.7, c = 130.2 A, beta = 103.6 degrees . Diffraction data were collected from a single crystal to 2.0 A.Entities:
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Year: 2004 PMID: 15502327 DOI: 10.1107/S0907444904021754
Source DB: PubMed Journal: Acta Crystallogr D Biol Crystallogr ISSN: 0907-4449